Protein misfolding underpins several fatal neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS) and Parkinson's disease (PD) (Cushman et al., 2010). In PD, α-synuclein (α-syn, α-syn, or α-synuclein) forms highly toxic prefibrillar oligomers and amyloid fibrils that accumulate in cytoplasmic Lewy bodies (Cushman et al., 2010). In ALS, TDP-43 or FUS accumulate in cytoplasmic inclusions in degenerating motor neurons (Robberecht and Philips, 2013). Unfortunately, treatments for these disorders are palliative and ineffective due to the apparent intractability of aggregated proteins. Effective therapies are urgently needed that eliminate the causative proteotoxic misfolded conformers via degradation or reactivation of the proteins to their native fold.